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Database: UniProt
Entry: A0A0S4IVK7_BODSA
LinkDB: A0A0S4IVK7_BODSA
Original site: A0A0S4IVK7_BODSA 
ID   A0A0S4IVK7_BODSA        Unreviewed;       892 AA.
AC   A0A0S4IVK7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE            EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN   ORFNames=BSAL_66915 {ECO:0000313|EMBL:CUF89536.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUF89536.1, ECO:0000313|Proteomes:UP000051952};
RN   [1] {ECO:0000313|Proteomes:UP000051952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC         Evidence={ECO:0000256|RuleBase:RU362083};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362083};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU362083}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIIA subfamily. {ECO:0000256|ARBA:ARBA00008804,
CC       ECO:0000256|RuleBase:RU362083}.
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DR   EMBL; CYKH01000435; CUF89536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4IVK7; -.
DR   VEuPathDB; TriTrypDB:BSAL_66915; -.
DR   OMA; GHFELVM; -.
DR   OrthoDB; 46741at2759; -.
DR   Proteomes; UP000051952; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0120029; P:proton export across plasma membrane; IEA:UniProtKB-UniRule.
DR   CDD; cd02076; P-type_ATPase_H; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006534; P-type_ATPase_IIIA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01647; ATPase-IIIA_H; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF48; PLASMA MEMBRANE ATPASE; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362083};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU362083};
KW   Ion transport {ECO:0000256|RuleBase:RU362083};
KW   Magnesium {ECO:0000256|RuleBase:RU362083};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362083};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362083};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362083};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362083};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362083}; Transport {ECO:0000256|RuleBase:RU362083}.
FT   TRANSMEM        39..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        217..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        250..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        617..640
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        652..676
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        688..716
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        736..754
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        774..793
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        813..830
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   DOMAIN          4..66
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          864..892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..882
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   892 AA;  98219 MW;  0F3CDA28E9800F51 CRC64;
     MDNDAPLLPP SHGLTTAEAE RLLAIHGRNE LPEKSTPGWV IFVRCLWGPM PIAIWIAVII
     EFALQNWPDG GILLFIQFAN ATIGWYETTK AGDAVAALRS SLKPLATAFR DGKWQNIDAG
     GIVPGDLVKL ASGSAVPADC SINEGQIDVD EAALTGESLP VTMSTEHMPK MGSTVVRGEV
     DGTVQYTGMK TFFGKTALLL QSVEADLGNI HYVLVRVMFV LTTLSLALCI ICFGYLMGHY
     KLSFKESLEF TVVLLVVSIP IAIEIVVTTT LALGSKELSI QKVIVTRLSA IEMMSAVNML
     CSDKTGTLTL NKMEIQEKCH TFEPGQNRAS VLVLAALAAK WREPPRDALD TMVLGAADLD
     ECDKFTQLEF VPFDPRLKRT EATLRGPDGF VFKVTKGAPN IVMELCHNKA EIKEDVEKII
     TDLGERGIRC LTVARTKEDG KWHMAGILTF LDPPRPDTKE TVRRSKEYGV DVKMITGDHQ
     LIAKEMARML DMDTNIMTSE GLPKFPESGD PKDIPLTLGD THGEMMLNCG GFAHVYPEHK
     YLIVETLRQR GYTCAMTGDG VNDSPALKRA DVGVAVHGAT DAARAASDMV LTEPGLSVVV
     DAMLIARGVF QRMLSFLTYR VSATLQLVFF FFIGVFALPL EHYGIIDPEF QFFHLPVLMF
     MLITLLNDGT LMAIGYDNVV PSSRPQRWNL PVLFTVAAVL AGVACVSSLL LLWMAVDSIR
     VYDKSWFHGL GIAQVQPGQI VTMVYLKVSI SDFLTLFSAR TQSDFFWSYA PSKILSIGAV
     LSLTISTIVA TFWPVDSPDG IKTIGLAHGD GNTNLLPIWV WLYCIFWWFV QDLTKVATYK
     ILDRYDLFNY RTIAQGEWTV ETARASQGKN SKKGKEQAEP LLREGKGYGS VN
//
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